3,653 research outputs found

    Beyond Higgs Couplings: Probing the Higgs with Angular Observables at Future e+e−e^+ e^- Colliders

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    We study angular observables in the e+e−→ZH→ℓ+ℓ− bbˉe^+e^-\to Z H\to \ell^+ \ell^-\,b\bar{b} channel at future circular e+e−e^+ e^- colliders such as CEPC and FCC-ee. Taking into account the impact of realistic cut acceptance and detector effects, we forecast the precision of six angular asymmetries at CEPC (FCC-ee) with center-of-mass energy s=\sqrt{s} = 240 GeV and 5 (30) ab−1{\rm ab}^{-1} integrated luminosity. We then determine the projected sensitivity to a range of operators relevant for the Higgs-strahlung process in the dimension-6 Higgs EFT. Our results show that angular observables provide complementary sensitivity to rate measurements when constraining various tensor structures arising from new physics. We further find that angular asymmetries provide a novel means of both probing BSM corrections to the HZγH Z \gamma coupling and constraining the "blind spot" in indirect limits on supersymmetric scalar top partners.Comment: 28 pages, 9 figures. v2: references added, matches published version in JHE

    Tyrosine/Cysteine Cluster Sensitizing Human γD-Crystallin to Ultraviolet Radiation-Induced Photoaggregation in Vitro

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    Ultraviolet radiation (UVR) exposure is a major risk factor for age-related cataract, a protein-aggregation disease of the human lens often involving the major proteins of the lens, the crystallins. γD-Crystallin (HγD-Crys) is abundant in the nucleus of the human lens, and its folding and aggregation have been extensively studied. Previous work showed that HγD-Crys photoaggregates in vitro upon exposure to UVA/UVB light and that its conserved tryptophans are not required for aggregation. Surprisingly, the tryptophan residues play a photoprotective role because of a distinctive energy-transfer mechanism. HγD-Crys also contains 14 tyrosine residues, 12 of which are organized as six pairs. We investigated the role of the tyrosines of HγD-Crys by replacing pairs with alanines and monitoring photoaggregation using light scattering and SDS-PAGE. Mutating both tyrosines in the Y16/Y28 pair to alanine slowed the formation of light-scattering aggregates. Further mutant studies implicated Y16 as important for photoaggregation. Mass spectrometry revealed that C18, in contact with Y16, is heavily oxidized during UVR exposure. Analysis of multiple mutant proteins by mass spectrometry suggested that Y16 and C18 likely participate in the same photochemical process. The data suggest an initial photoaggregation pathway for HγD-Crys in which excited-state Y16 interacts with C18, initiating radical polymerization.National Eye Institute (EY015834

    Electron-Beam Driven Relaxation Oscillations in Ferroelectric Nanodisks

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    Using a combination of computational simulations, atomic-scale resolution imaging and phenomenological modelling, we examine the underlying mechanism for nanodomain restructuring in lead zirconate titanate (PZT) nanodisks driven by electron beams. The observed subhertz nanodomain dynamics are identified with relaxation oscillations where the charging/discharging cycle time is determined by saturation of charge traps and nanodomain wall creep. These results are unusual in that they indicate very slow athermal dynamics in nanoscale systems.Comment: 5 pages, 2 figure
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